ID ZC3HD_HUMAN Reviewed; 1668 AA. AC Q5T200; A2A323; O94936; Q5T1Z9; Q7Z7J3; Q8NDT6; Q9H0L6; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Zinc finger CCCH domain-containing protein 13 {ECO:0000305}; GN Name=ZC3H13 {ECO:0000303|PubMed:29507755, GN ECO:0000312|HGNC:HGNC:20368}; GN Synonyms=KIAA0853 {ECO:0000303|PubMed:10048485}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ASP-1429. RA Shan Y.X., Yu L.; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-971, AND VARIANT ASP-1429. RC TISSUE=Fetal brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-1668 (ISOFORM 2), AND VARIANT RP ASP-1429. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 702-1668 (ISOFORM 1), AND VARIANT RP ASP-1429. RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263 AND SER-265, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; THR-263 AND SER-265, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; THR-263; SER-265 AND RP SER-993, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-209; SER-242; RP SER-316; SER-318; SER-325; THR-354; THR-364; SER-370; SER-372; SER-381; RP SER-831; SER-833; SER-837; SER-845; SER-848; SER-853; SER-875; SER-877; RP SER-986; SER-993; SER-1010; SER-1014 AND SER-1017, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-1453; SER-1456 AND SER-1466 (ISOFORM 2), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; THR-263; SER-986; RP SER-993; SER-1014 AND SER-1017, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-198; SER-207; RP SER-209; SER-242; THR-263; SER-265; SER-370; SER-372; SER-381; SER-845; RP SER-848; SER-853; SER-877; SER-993; SER-1010; SER-1014; SER-1017; THR-1170; RP SER-1208; SER-1230; SER-1364; SER-1366 AND SER-1438, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; THR-237; SER-242; RP THR-263; SER-265; SER-325; SER-328; SER-370; SER-372; SER-381; SER-845; RP SER-848; SER-853; SER-877; THR-882; SER-986; SER-993; SER-1010; SER-1017; RP SER-1191; SER-1194; SER-1208; SER-1210 AND SER-1465, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP IDENTIFICATION IN A MACOM-LIKE COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=24100041; DOI=10.1074/jbc.m113.500397; RA Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T., RA Hamakubo T.; RT "Identification of Wilms' tumor 1-associating protein complex and its role RT in alternative splicing and the cell cycle."; RL J. Biol. Chem. 288:33292-33302(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-198; SER-207; RP SER-209; SER-211; SER-238; SER-242; THR-263; SER-265; SER-318; SER-325; RP SER-370; SER-372; SER-381; SER-643; SER-873; SER-875; SER-877; SER-943; RP SER-986; SER-993; THR-1033; THR-1170; SER-1364; SER-1366; SER-1386; RP SER-1406 AND SER-1409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-370; SER-372; RP SER-877; SER-1010; SER-1014; SER-1017 AND SER-1210, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-194, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [23] RP FUNCTION, AND IDENTIFICATION IN THE WMM COMPLEX. RX PubMed=29507755; DOI=10.1038/s41421-018-0019-0; RA Yue Y., Liu J., Cui X., Cao J., Luo G., Zhang Z., Cheng T., Gao M., Shu X., RA Ma H., Wang F., Wang X., Shen B., Wang Y., Feng X., He C., Liu J.; RT "VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop RT codon and associates with alternative polyadenylation."; RL Cell Discov. 4:10-10(2018). CC -!- FUNCTION: Associated component of the WMM complex, a complex that CC mediates N6-methyladenosine (m6A) methylation of RNAs, a modification CC that plays a role in the efficiency of mRNA splicing and RNA processing CC (PubMed:29507755). Acts as a key regulator of m6A methylation by CC promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). CC Controls embryonic stem cells (ESCs) pluripotency via its role in m6A CC methylation (By similarity). In the WMM complex, anchors component of CC the MACOM subcomplex in the nucleus (By similarity). Also required for CC bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By CC similarity). {ECO:0000250|UniProtKB:E9Q784}. CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex CC composed of a catalytic subcomplex, named MAC, and of an associated CC subcomplex, named MACOM (PubMed:29507755). The MAC subcomplex is CC composed of METTL3 and METTL14. The MACOM subcomplex is composed of CC WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or CC RBM15B) (PubMed:29507755). Also a component of a MACOM-like complex, CC named WTAP complex, composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, CC RBM15, BCLAF1 and THRAP3 (PubMed:24100041). CC {ECO:0000269|PubMed:24100041, ECO:0000269|PubMed:29507755}. CC -!- INTERACTION: CC Q5T200; P0DPB3: SCHIP1; NbExp=2; IntAct=EBI-2679720, EBI-1397509; CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24100041}. CC Nucleus, nucleoplasm {ECO:0000269|PubMed:24100041}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5T200-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5T200-2; Sequence=VSP_027202, VSP_014252, VSP_014253; CC -!- SIMILARITY: Belongs to the ZC3H13 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY283618; AAP37483.1; -; mRNA. DR EMBL; AL157758; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445232; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL831833; CAD38544.1; -; mRNA. DR EMBL; AL136745; CAB66679.2; -; mRNA. DR EMBL; AB020660; BAA74876.1; -; mRNA. DR CCDS; CCDS81766.1; -. [Q5T200-1] DR CCDS; CCDS9400.1; -. [Q5T200-2] DR RefSeq; NP_001070256.1; NM_001076788.1. DR RefSeq; NP_001317493.1; NM_001330564.1. DR RefSeq; NP_001317494.1; NM_001330565.1. [Q5T200-1] DR RefSeq; NP_001317495.1; NM_001330566.1. [Q5T200-1] DR RefSeq; NP_001317496.1; NM_001330567.1. [Q5T200-1] DR RefSeq; NP_055885.3; NM_015070.5. [Q5T200-2] DR RefSeq; XP_005266369.1; XM_005266312.1. DR PDB; 7VF2; EM; 3.00 A; B=1106-1668. DR PDBsum; 7VF2; -. DR AlphaFoldDB; Q5T200; -. DR EMDB; EMD-31946; -. DR SMR; Q5T200; -. DR BioGRID; 116719; 147. DR ComplexPortal; CPX-1605; WMM N6-adenosine-methyltransferase complex. DR CORUM; Q5T200; -. DR IntAct; Q5T200; 28. DR MINT; Q5T200; -. DR STRING; 9606.ENSP00000242848; -. DR GlyGen; Q5T200; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q5T200; -. DR PhosphoSitePlus; Q5T200; -. DR BioMuta; ZC3H13; -. DR DMDM; 68052314; -. DR EPD; Q5T200; -. DR jPOST; Q5T200; -. DR MassIVE; Q5T200; -. DR MaxQB; Q5T200; -. DR PaxDb; 9606-ENSP00000282007; -. DR PeptideAtlas; Q5T200; -. DR ProteomicsDB; 64298; -. [Q5T200-1] DR ProteomicsDB; 64299; -. [Q5T200-2] DR Pumba; Q5T200; -. DR Antibodypedia; 23654; 132 antibodies from 22 providers. DR DNASU; 23091; -. DR Ensembl; ENST00000242848.8; ENSP00000242848.4; ENSG00000123200.17. [Q5T200-1] DR Ensembl; ENST00000282007.7; ENSP00000282007.3; ENSG00000123200.17. [Q5T200-2] DR GeneID; 23091; -. DR KEGG; hsa:23091; -. DR UCSC; uc001vas.3; human. [Q5T200-1] DR AGR; HGNC:20368; -. DR CTD; 23091; -. DR DisGeNET; 23091; -. DR GeneCards; ZC3H13; -. DR HGNC; HGNC:20368; ZC3H13. DR HPA; ENSG00000123200; Low tissue specificity. DR MIM; 616453; gene. DR neXtProt; NX_Q5T200; -. DR OpenTargets; ENSG00000123200; -. DR PharmGKB; PA134907656; -. DR VEuPathDB; HostDB:ENSG00000123200; -. DR eggNOG; KOG1874; Eukaryota. DR GeneTree; ENSGT00730000111163; -. DR HOGENOM; CLU_003683_0_0_1; -. DR InParanoid; Q5T200; -. DR OrthoDB; 3062202at2759; -. DR PhylomeDB; Q5T200; -. DR TreeFam; TF332670; -. DR PathwayCommons; Q5T200; -. DR SignaLink; Q5T200; -. DR BioGRID-ORCS; 23091; 236 hits in 1167 CRISPR screens. DR ChiTaRS; ZC3H13; human. DR GeneWiki; ZC3H13; -. DR GenomeRNAi; 23091; -. DR Pharos; Q5T200; Tbio. DR PRO; PR:Q5T200; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q5T200; Protein. DR Bgee; ENSG00000123200; Expressed in sural nerve and 214 other cell types or tissues. DR ExpressionAtlas; Q5T200; baseline and differential. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0080009; P:mRNA methylation; IMP:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:2000036; P:regulation of stem cell population maintenance; ISS:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1. DR InterPro; IPR000571; Znf_CCCH. DR InterPro; IPR036855; Znf_CCCH_sf. DR PANTHER; PTHR13585; CHASCON, ISOFORM D-RELATED; 1. DR PANTHER; PTHR13585:SF19; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 13; 1. DR Pfam; PF00642; zf-CCCH; 1. DR SMART; SM00356; ZnF_C3H1; 1. DR SUPFAM; SSF90229; CCCH zinc finger; 1. DR PROSITE; PS50103; ZF_C3H1; 1. DR Genevisible; Q5T200; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Developmental protein; KW Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..1668 FT /note="Zinc finger CCCH domain-containing protein 13" FT /id="PRO_0000050778" FT ZN_FING 36..64 FT /note="C3H1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT REGION 1..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 56..157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 190..1112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1125..1466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 645..789 FT /evidence="ECO:0000255" FT COILED 1300..1366 FT /evidence="ECO:0000255" FT COMPBIAS 13..38 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..157 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..251 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 275..318 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 319..345 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 352..388 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 390..573 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 578..597 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 598..867 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 878..981 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1008..1027 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1053..1081 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1096..1110 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1125..1153 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1154..1187 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1188..1211 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1212..1450 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 211 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 237 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 238 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 242 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 263 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:15144186, FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15144186, FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 318 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 354 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 364 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 372 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 381 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 643 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 831 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 833 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 837 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 845 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 848 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 853 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 873 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 875 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 877 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 882 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 943 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 986 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 993 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1010 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1014 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1017 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 1033 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1170 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1191 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1208 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1210 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1230 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1364 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1366 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1382 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 1386 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1406 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1438 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1465 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 179 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 194 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1440 FT /note="E -> EA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.1" FT /id="VSP_027202" FT VAR_SEQ 1558..1563 FT /note="DADNLF -> GSFILL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.1" FT /id="VSP_014252" FT VAR_SEQ 1564..1668 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.1" FT /id="VSP_014253" FT VARIANT 1429 FT /note="E -> D (in dbSNP:rs9534264)" FT /evidence="ECO:0000269|PubMed:10048485, FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:17974005, FT ECO:0000269|Ref.1" FT /id="VAR_022727" FT CONFLICT 702..704 FT /note="EKE -> KAR (in Ref. 5; BAA74876)" FT /evidence="ECO:0000305" FT CONFLICT 967 FT /note="I -> K (in Ref. 3; CAD38544)" FT /evidence="ECO:0000305" FT STRAND 1505..1508 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1518..1521 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1523..1530 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1534..1537 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1539..1550 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1556..1560 FT /evidence="ECO:0007829|PDB:7VF2" FT STRAND 1565..1567 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1568..1582 FT /evidence="ECO:0007829|PDB:7VF2" FT TURN 1583..1586 FT /evidence="ECO:0007829|PDB:7VF2" FT STRAND 1589..1592 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1597..1607 FT /evidence="ECO:0007829|PDB:7VF2" FT HELIX 1627..1642 FT /evidence="ECO:0007829|PDB:7VF2" FT MOD_RES Q5T200-2:1453 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q5T200-2:1456 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q5T200-2:1466 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 1668 AA; 196635 MW; B7E8118D3B5954D6 CRC64; MSKIRRKVTV ENTKTISDST SRRPSVFERL GPSTGSTAET QCRNWLKTGN CLYGNTCRFV HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDTEP QKRNTEESSS PVRKESSRGR HREKEDIKIT KERTPESEEE NVEWETNRDD SDNGDINYDY VHELSLEMKR QKIQRELMKL EQENMEKREE IIIKKEVSPE VVRSKLSPSP SLRKSSKSPK RKSSPKSSSA SKKDRKTSAV SSPLLDQQRN SKTNQSKKKG PRTPSPPPPI PEDIALGKKY KEKYKVKDRI EEKTRDGKDR GRDFERQREK RDKPRSTSPA GQHHSPISSR HHSSSSQSGS SIQRHSPSPR RKRTPSPSYQ RTLTPPLRRS ASPYPSHSLS SPQRKQSPPR HRSPMREKGR HDHERTSQSH DRRHERREDT RGKRDREKDS REEREYEQDQ SSSRDHRDDR EPRDGRDRRD ARDTRDRREL RDSRDMRDSR EMRDYSRDTK ESRDPRDSRS TRDAHDYRDR EGRDTHRKED TYPEESRSYG RNHLREESSR TEIRNESRNE SRSEIRNDRM GRSRGRVPEL PEKGSRGSRG SQIDSHSSNS NYHDSWETRS SYPERDRYPE RDNRDQARDS SFERRHGERD RRDNRERDQR PSSPIRHQGR NDELERDERR EERRVDRVDD RRDERARERD RERERDRERE RERERERDRE REKERELERE RARERERERE KERDRERDRD RDHDRERERE RERDREKERE REREERERER ERERERERER ERERERARER DKERERQRDW EDKDKGRDDR REKREEIRED RNPRDGHDER KSKKRYRNEG SPSPRQSPKR RREHSPDSDA YNSGDDKNEK HRLLSQVVRP QESRSLSPSH LTEDRQGRWK EEDRKPERKE SSRRYEEQEL KEKVSSVDKQ REQTEILESS RMRAQDIIGH HQSEDRETSD RAHDENKKKA KIQKKPIKKK KEDDVGIERG NIETTSEDGQ VFSPKKGQKK KSIEKKRKKS KGDSDISDEE AAQQSKKKRG PRTPPITTKE ELVEMCNGKN GILEDSQKKE DTAFSDWSDE DVPDRTEVTE AEHTATATTP GSTPSPLSSL LPPPPPVATA TATTVPATLA ATTAAAATSF STSAITISTS ATPTNTTNNT FANEDSHRKC HRTRVEKVET PHVTIEDAQH RKPMDQKRSS SLGSNRSNRS HTSGRLRSPS NDSAHRSGDD QSGRKRVLHS GSRDREKTKS LEITGERKSR IDQLKRGEPS RSTSSDRQDS RSHSSRRSSP ESDRQVHSRS GSFDSRDRLQ ERDRYEHDRE RERERRDTRQ REWDRDADKD WPRNRDRDRL RERERERERD KRRDLDRERE RLISDSVERD RDRDRDRTFE SSQIESVKRC EAKLEGEHER DLESTSRDSL ALDKERMDKD LGSVQGFEET NKSERTESLE GDDESKLDDA HSLGSGAGEG YEPISDDELD EILAGDAEKR EDQQDEEKMP DPLDVIDVDW SGLMPKHPKE PREPGAALLK FTPGAVMLRV GISKKLAGSE LFAKVKETCQ RLLEKPKDAD NLFEHELGAL NMAALLRKEE RASLLSNLGP CCKALCFRRD SAIRKQLVKN EKGTIKQAYT SAPMVDNELL RLSLRLFKRK TTCHAPGHEK TEDNKLSQSS IQQELCVS //